ArticleJournal of bacteriology1997
Metals control activity and expression of the heme biosynthesis enzyme delta-aminolevulinic acid dehydratase in Bradyrhizobium japonicum.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 37 citations in OpenAlex.
- Two TonB-dependent outer membrane transporters involved in heme uptake inMicrobial cell (Graz, Austria) · 2024Article
- Production of copropophyrin III, biliverdin and bilirubin by the rufomycin producer,Frontiers in microbiology · 2023Article
- Genetic susceptibility of δ-ALAD associated with lead (Pb) intoxication: sources of exposure, preventive measures, and treatment interventions.Environmental science and pollution research international · 2021Review
- Genetic regulators of mineral amount in Nelore cattle muscle predicted by a new co-expression and regulatory impact factor approach.Scientific reports · 2020Article
- Interdependence of tetrapyrrole metabolism, the generation of oxidative stress and the mitigative oxidative stress response.Redox biology · 2015Review
- Environmental contaminants perturb fragile protein assemblies and inhibit normal protein function.Current chemical biology · 2013Article
- delta-Aminolevulinic acid dehydratase of Haloarcula argentinensis isolated from Tuz Lake in Turkey.Environmental monitoring and assessment · 2010Article
- Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other Alpha-proteobacteria.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2009Article
- The Bradyrhizobium japonicum Fur protein is an iron-responsive regulator in vivo.Molecular genetics and genomics : MGG · 2006Article
- Iron-dependent cytochrome c1 expression is mediated by the status of heme in Bradyrhizobium japonicum.Journal of bacteriology · 2005Article
- Parasite plastids: maintenance and functions.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2003Article
- BhuR, a virulence-associated outer membrane protein of Bordetella avium, is required for the acquisition of iron from heme and hemoproteins.Infection and immunity · 2002Article
- One of two hemN genes in Bradyrhizobium japonicum is functional during anaerobic growth and in symbiosis.Journal of bacteriology · 2001Article
- Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heme biosynthesis enzyme delta-aminolevulinic acid dehydratase (ALAD) requires magnesium or zinc for activity, depending on the organism, and the heme moiety contains iron. Thus, metals are important for heme formation in at least two different ways. Bradyrhizobium japonicum ALAD* is an engineered derivative of wild-type ALAD that requires Zn2+ for activity rather than Mg2+ (S. Chauhan and M. R. O'Brian, J. Biol. Chem. 270:19823-19827, 1995). The pH optimum for ALAD* activity was over 3.5 units lower than for that of the wild-type enzyme, and ALAD* activity was inhibited by lead and cadmium, as reported for the zinc-containing dehydratases of animals. In addition, ALAD* was significantly more thermostable than ALAD; the temperature optima are 50 and 37 degrees C, respectively. These observations strongly suggest that the metal contributes to both catalysis and structure, and this conclusion may be extrapolated to ALADs in general. Although iron did not affect the activity of the preformed protein, enzyme assays and immunoblot analysis demonstrated that the iron concentration in which the cells were grown had a strong positive effect on ALAD activity and the protein level. RNase protection analysis showed that the transcript quantity of hemB, the gene encoding ALAD, was iron dependent; thus, iron regulates hemB at the mRNA level. Induction of hemB mRNA in response to iron was rapid, suggesting that the factor(s) needed to mediate iron control was present in iron-limited cells and did not need to be synthesized de novo. ALAD protein levels and enzyme activities were similar in cells of the wild type and a heme-defective strain, indicating that control by iron is not an indirect effect of the cellular heme status. We conclude that the heme biosynthetic pathway is coordinated with cellular iron levels and that this control may prevent the accumulation of toxic porphyrin intermediates.
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